Evidence map›Paper›PMID 34149429›Full record

ArticleFrontiers in pharmacology2021

Discovery of New Potent anti-MERS CoV Fusion Inhibitors.

Mahmoud Kandeel, Mizuki Yamamoto, Byoung Kwon Park, Abdulla Al-Taher, Aya Watanabe, Jin Gohda, Yasushi Kawaguchi, Kentaro Oh-Hashi, Hyung-Joo Kwon, Jun-Ichiro Inoue

Open access · goldAbstract read
In one paragraph

Article in Frontiers in pharmacology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
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  4. Omicron variant genome evolution and phylogenetics.Journal of medical virology · 2022
    Article
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  8. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 4 countries.

Mahmoud KandeelDepartment of Biomedical Sciences, College of Veterinary Medicine, King Faisal University, Al-Ahsa, Saudi Arabia.
Mizuki YamamotoResearch Center for Asian Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Byoung Kwon ParkDepartment of Microbiology, Hallym University College of Medicine, Chuncheon, South Korea.
Abdulla Al-TaherDepartment of Biomedical Sciences, College of Veterinary Medicine, King Faisal University, Al-Ahsa, Saudi Arabia.
Aya WatanabeDivision of Cellular and Molecular Biology, Department of Cancer Biology, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
Jin GohdaResearch Center for Asian Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Yasushi KawaguchiResearch Center for Asian Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Kentaro Oh-HashiDepartment of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University, Gifu, Japan.
Hyung-Joo KwonDepartment of Microbiology, Hallym University College of Medicine, Chuncheon, South Korea.
Jun-Ichiro InoueDivision of Cellular and Molecular Biology, Department of Cancer Biology, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
The University of Tokyo · JPHallym University · KRKing Faisal University · SANational Institute of Infectious Diseases · JPGifu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV), capable of zoonotic transmission, has been associated with emerging viral pneumonia in humans. In this study, a set of highly potent peptides were designed to prevent MERS-CoV fusion through competition with heptad repeat domain 2 (HR2) at its HR1 binding site. We designed eleven peptides with stronger estimated HR1 binding affinities than the wild-type peptide to prevent viral fusion with the cell membrane. Eight peptides showed strong inhibition of spike-mediated MERS-CoV cell-cell fusion with IC50 values in the nanomolar range (0.25-2.3 µM). Peptides #4-6 inhibited 95-98.3% of MERS-CoV plaque formation. Notably, peptide four showed strong inhibition of MERS-CoV plaques formation with EC50 = 0.302 µM. All peptides demonstrated safe profiles without cytotoxicity up to a concentration of 10 μM, and this cellular safety, combined with their anti-MERS-CoV antiviral activity, indicate all peptides can be regarded as potential promising antiviral agents.

Indexed as

antiviralscoronavirusdrug discoveryfusion inhibitorsMERS-CoV

Identifiers

PMID34149429
PMCPMC8206564
OpenAlexW3172157766

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.